|
Name |
Accession |
Description |
Interval |
E-value |
| BAH_BAHCC1 |
cd04714 |
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2816-2960 |
5.06e-57 |
|
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.
:
Pssm-ID: 240065 Cd Length: 121 Bit Score: 193.77 E-value: 5.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2816 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhqgqhwdqkssrslpaalrvssqR 2895
Cdd:cd04714 1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217368908 2896 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2960
Cdd:cd04714 56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
|
|
| Tudor_TNRC18 |
cd20469 |
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ... |
2220-2286 |
4.77e-37 |
|
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar proteins; TNRC18, also called long CAG trinucleotide repeat-containing gene 79 protein (CAGL79), is a protein that in humans is encoded by the TNRC18 gene. Its biological function remains unclear. TNRC18 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
:
Pssm-ID: 410540 Cd Length: 67 Bit Score: 134.47 E-value: 4.77e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 2220 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2286
Cdd:cd20469 1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
2291-2531 |
7.63e-06 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2291 PSPALLVPSAKRRSRKTSKdtgegkdggtAGSEEPGAKARGRGRKPSAKAKGDRAATleegnPTDEVPSTPLALEPSSTP 2370
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPR----------PAPRPSEPAVTSRARRPDAPPQSARPRA-----PVDDRGDPRGPAPPSPLP 2618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2371 GSKKSPPEPVDKRAKAPKARPAPPQPSPAPPAFTSCPAPEPFAELPAPATSLAPAPLITMPATRPKPKKARAAEESGAKG 2450
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2451 PRRPGEEAEllvkldhegvTSPKSKKAKEALLLREDPGAGGWQEPKSLLSLGSYPPAAGSSEPKAPWPKATDGDLAQEPG 2530
Cdd:PHA03247 2699 ADPPPPPPT----------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
|
.
gi 2217368908 2531 P 2531
Cdd:PHA03247 2769 P 2769
|
|
| PksD super family |
cl43841 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
251-797 |
3.73e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
The actual alignment was detected with superfamily member COG3321:
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.40 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 251 QDRGPPRLAERLSPFLAESKTKNAALQPSVLTMCNGGAGDVGLPALVAEAGRGGAKEAARQDEGARLLRRTETLLPGPRP 330
Cdd:COG3321 854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 331 CPSPLPPPPAPPKGPPAPPAATPAGVYTVFREQGREHRVVAPTFVPSVEAFDERPGPIQIASQARDARAREREAGRPGVL 410
Cdd:COG3321 934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 411 QAPPGSPRPLDRPEGLREKNSVIRSLKRPPPADAPTVRATRASPDPRAYVPAKELLKPEADPRPCERAPRGPAGPAAQQA 490
Cdd:COG3321 1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 491 AKLFGLEPGRPPPtgpehkwkpfelgnfAATQMAVLAAQHHHSRAEEEAAVVAASSSKKAYLDPGAVLPRSAATCGRPVA 570
Cdd:COG3321 1094 ALALALAALAAAL---------------LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAA 1158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 571 DMHSAAHGSGEASAMQSLIKYSGSFARDAVAVRPGGCGKKSPFGGLGTMKPEPAPTSAGASRAQARLPHSGGPAAGGGRQ 650
Cdd:COG3321 1159 LAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLAL 1238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 651 LKRDPERPESAKAFGREGSGAQGEAEVRHPPVGIAVAVARQKDSGGSGRLGPGLVDQERSLSLSnVKGHGRADEDCVDDR 730
Cdd:COG3321 1239 AAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALL-AAAAAAAAAAAAAAA 1317
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 731 ARHREERLLGARLDRDQEKLLRESKELADLARLHPTSCAPNGLNPNLMVTGGPALAGSGRWSADPAA 797
Cdd:COG3321 1318 AAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BAH_BAHCC1 |
cd04714 |
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2816-2960 |
5.06e-57 |
|
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.
Pssm-ID: 240065 Cd Length: 121 Bit Score: 193.77 E-value: 5.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2816 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhqgqhwdqkssrslpaalrvssqR 2895
Cdd:cd04714 1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217368908 2896 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2960
Cdd:cd04714 56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
|
|
| Tudor_TNRC18 |
cd20469 |
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ... |
2220-2286 |
4.77e-37 |
|
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar proteins; TNRC18, also called long CAG trinucleotide repeat-containing gene 79 protein (CAGL79), is a protein that in humans is encoded by the TNRC18 gene. Its biological function remains unclear. TNRC18 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410540 Cd Length: 67 Bit Score: 134.47 E-value: 4.77e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 2220 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2286
Cdd:cd20469 1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
|
|
| BAH |
smart00439 |
Bromo adjacent homology domain; |
2818-2956 |
1.78e-13 |
|
Bromo adjacent homology domain;
Pssm-ID: 214664 [Multi-domain] Cd Length: 121 Bit Score: 69.24 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2818 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHqgqhwdqkssrslpaalrvssqr 2895
Cdd:smart00439 1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217368908 2896 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2956
Cdd:smart00439 58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
|
|
| BAH |
pfam01426 |
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ... |
2817-2956 |
2.81e-10 |
|
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.
Pssm-ID: 460207 Cd Length: 120 Bit Score: 60.01 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2817 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEET--SPGKQFHqgqhwdqkssrslpaalrvss 2893
Cdd:pfam01426 1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETvhRAGKAFN--------------------- 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217368908 2894 qrkdfmERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2956
Cdd:pfam01426 60 ------KDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKI--KEPDDFFCELLYDPKTK 114
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2291-2531 |
7.63e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2291 PSPALLVPSAKRRSRKTSKdtgegkdggtAGSEEPGAKARGRGRKPSAKAKGDRAATleegnPTDEVPSTPLALEPSSTP 2370
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPR----------PAPRPSEPAVTSRARRPDAPPQSARPRA-----PVDDRGDPRGPAPPSPLP 2618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2371 GSKKSPPEPVDKRAKAPKARPAPPQPSPAPPAFTSCPAPEPFAELPAPATSLAPAPLITMPATRPKPKKARAAEESGAKG 2450
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2451 PRRPGEEAEllvkldhegvTSPKSKKAKEALLLREDPGAGGWQEPKSLLSLGSYPPAAGSSEPKAPWPKATDGDLAQEPG 2530
Cdd:PHA03247 2699 ADPPPPPPT----------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
|
.
gi 2217368908 2531 P 2531
Cdd:PHA03247 2769 P 2769
|
|
| Tudor_3 |
pfam18115 |
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ... |
2228-2280 |
1.60e-05 |
|
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2.
Pssm-ID: 436284 Cd Length: 50 Bit Score: 44.47 E-value: 1.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217368908 2228 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2280
Cdd:pfam18115 1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
251-797 |
3.73e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.40 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 251 QDRGPPRLAERLSPFLAESKTKNAALQPSVLTMCNGGAGDVGLPALVAEAGRGGAKEAARQDEGARLLRRTETLLPGPRP 330
Cdd:COG3321 854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 331 CPSPLPPPPAPPKGPPAPPAATPAGVYTVFREQGREHRVVAPTFVPSVEAFDERPGPIQIASQARDARAREREAGRPGVL 410
Cdd:COG3321 934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 411 QAPPGSPRPLDRPEGLREKNSVIRSLKRPPPADAPTVRATRASPDPRAYVPAKELLKPEADPRPCERAPRGPAGPAAQQA 490
Cdd:COG3321 1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 491 AKLFGLEPGRPPPtgpehkwkpfelgnfAATQMAVLAAQHHHSRAEEEAAVVAASSSKKAYLDPGAVLPRSAATCGRPVA 570
Cdd:COG3321 1094 ALALALAALAAAL---------------LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAA 1158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 571 DMHSAAHGSGEASAMQSLIKYSGSFARDAVAVRPGGCGKKSPFGGLGTMKPEPAPTSAGASRAQARLPHSGGPAAGGGRQ 650
Cdd:COG3321 1159 LAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLAL 1238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 651 LKRDPERPESAKAFGREGSGAQGEAEVRHPPVGIAVAVARQKDSGGSGRLGPGLVDQERSLSLSnVKGHGRADEDCVDDR 730
Cdd:COG3321 1239 AAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALL-AAAAAAAAAAAAAAA 1317
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 731 ARHREERLLGARLDRDQEKLLRESKELADLARLHPTSCAPNGLNPNLMVTGGPALAGSGRWSADPAA 797
Cdd:COG3321 1318 AAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BAH_BAHCC1 |
cd04714 |
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2816-2960 |
5.06e-57 |
|
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.
Pssm-ID: 240065 Cd Length: 121 Bit Score: 193.77 E-value: 5.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2816 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhqgqhwdqkssrslpaalrvssqR 2895
Cdd:cd04714 1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217368908 2896 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2960
Cdd:cd04714 56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
|
|
| Tudor_TNRC18 |
cd20469 |
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ... |
2220-2286 |
4.77e-37 |
|
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar proteins; TNRC18, also called long CAG trinucleotide repeat-containing gene 79 protein (CAGL79), is a protein that in humans is encoded by the TNRC18 gene. Its biological function remains unclear. TNRC18 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410540 Cd Length: 67 Bit Score: 134.47 E-value: 4.77e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 2220 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2286
Cdd:cd20469 1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
|
|
| Tudor_BAHCC1-like |
cd20397 |
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ... |
2220-2285 |
4.19e-30 |
|
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The family of BAHCC1 includes BAHCC1 and trinucleotide repeat-containing gene 18 protein (TNRC18). BAHCC1 may function as a transcriptional regulator. The biological function of TNRC18 remains unclear. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410468 Cd Length: 67 Bit Score: 114.73 E-value: 4.19e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 2220 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDD-GDLITVEFDDGDTGRIPLSHIRLLPPDYK 2285
Cdd:cd20397 1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDSqEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
|
|
| Tudor_BAHCC1 |
cd20470 |
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ... |
2218-2285 |
6.67e-25 |
|
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410541 Cd Length: 70 Bit Score: 100.26 E-value: 6.67e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2218 PASTRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDL--ITVEFDDGDTGRIPLSHIRLLPPDYK 2285
Cdd:cd20470 1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGIDEEDDEdsVMVEFDDGDRGRISVSNIRLLPPDYK 70
|
|
| BAH |
cd04370 |
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ... |
2816-2956 |
8.35e-22 |
|
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.
Pssm-ID: 239835 [Multi-domain] Cd Length: 123 Bit Score: 93.23 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2816 KEMIRIGDCAVFLSAG--RPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKQFHQGqhwdqkssrslpaalrvss 2893
Cdd:cd04370 1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFAL------------------- 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217368908 2894 qrkdfmERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMlKTKKYQDSEGLYYLAGTYEPTTG 2956
Cdd:cd04370 62 ------RRELFLSDHLDEIPVESIIGKCKVLFVSEFEGL-KQRPNKIDTDDFFCRLAYDPTTK 117
|
|
| BAH |
smart00439 |
Bromo adjacent homology domain; |
2818-2956 |
1.78e-13 |
|
Bromo adjacent homology domain;
Pssm-ID: 214664 [Multi-domain] Cd Length: 121 Bit Score: 69.24 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2818 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHqgqhwdqkssrslpaalrvssqr 2895
Cdd:smart00439 1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217368908 2896 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2956
Cdd:smart00439 58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
|
|
| BAH |
pfam01426 |
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ... |
2817-2956 |
2.81e-10 |
|
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.
Pssm-ID: 460207 Cd Length: 120 Bit Score: 60.01 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2817 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEET--SPGKQFHqgqhwdqkssrslpaalrvss 2893
Cdd:pfam01426 1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETvhRAGKAFN--------------------- 59
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217368908 2894 qrkdfmERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2956
Cdd:pfam01426 60 ------KDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKI--KEPDDFFCELLYDPKTK 114
|
|
| BAH_polybromo |
cd04717 |
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ... |
2818-2871 |
3.09e-07 |
|
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.
Pssm-ID: 240068 Cd Length: 121 Bit Score: 51.43 E-value: 3.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217368908 2818 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEET--SPGKQF 2871
Cdd:cd04717 3 QYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETfhEPTRKF 58
|
|
| BAH_plant_3 |
cd04713 |
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ... |
2801-2937 |
6.21e-07 |
|
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.
Pssm-ID: 240064 Cd Length: 146 Bit Score: 51.31 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2801 KGKARKLFYKAIVRGKEMIRIGDCAVFLSA-GRPnlPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhqGQHWDQ 2879
Cdd:cd04713 3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKK----GGNWKA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217368908 2880 KSSRSlpaalrvssqrkdfmeraLYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKK 2937
Cdd:cd04713 77 EDPRE------------------LFYSFHRDEVPAESVLHPCKVAFVPKGKQIPLRKG 116
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2291-2531 |
7.63e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2291 PSPALLVPSAKRRSRKTSKdtgegkdggtAGSEEPGAKARGRGRKPSAKAKGDRAATleegnPTDEVPSTPLALEPSSTP 2370
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPR----------PAPRPSEPAVTSRARRPDAPPQSARPRA-----PVDDRGDPRGPAPPSPLP 2618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2371 GSKKSPPEPVDKRAKAPKARPAPPQPSPAPPAFTSCPAPEPFAELPAPATSLAPAPLITMPATRPKPKKARAAEESGAKG 2450
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2451 PRRPGEEAEllvkldhegvTSPKSKKAKEALLLREDPGAGGWQEPKSLLSLGSYPPAAGSSEPKAPWPKATDGDLAQEPG 2530
Cdd:PHA03247 2699 ADPPPPPPT----------PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768
|
.
gi 2217368908 2531 P 2531
Cdd:PHA03247 2769 P 2769
|
|
| Tudor_3 |
pfam18115 |
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ... |
2228-2280 |
1.60e-05 |
|
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2.
Pssm-ID: 436284 Cd Length: 50 Bit Score: 44.47 E-value: 1.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217368908 2228 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2280
Cdd:pfam18115 1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
|
|
| BAH_MTA |
cd04709 |
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ... |
2818-2963 |
7.26e-05 |
|
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.
Pssm-ID: 240060 Cd Length: 164 Bit Score: 45.85 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2818 MIRIGDCAVFLSAgrPNLPY-IGRIQSMWESWGNNMVVRVKWFYHPEETSPgkqfHQGQHWDQKSSRSLPAALRVSS-QR 2895
Cdd:cd04709 3 MYRVGDYVYFESS--PNNPYlIRRIEELNKTARGHVEAKVVCYYRRRDIPD----SLYQLADQHRRELEEKSDDLTPkQR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217368908 2896 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKYQDSegLYYLAGtYEPTTGMIFSTDG 2963
Cdd:cd04709 77 HQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDT--FFYSLV-YDPEQKTLLADQG 141
|
|
| Tudor_SpCrb2-like_rpt1 |
cd20395 |
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ... |
2227-2280 |
1.07e-04 |
|
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and similar proteins; Crb2, also called RAD9 protein homolog, or checkpoint mediator protein crb2, is a DNA repair protein essential for cell cycle arrest at the G1 and G2 stages following DNA damage by X-, and UV-irradiation, or inactivation of DNA ligase. Crb2 contains two Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410466 Cd Length: 50 Bit Score: 41.96 E-value: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2217368908 2227 GTRIAAYWSQqYRCLYPGTVVrglldLEDDGDLITVEFDDGDTGRIPLSHIRLL 2280
Cdd:cd20395 1 PTRVLAFWKG-DGNYYPATIV-----GPVSSSAYKVQFDDGTSSSVPPTQIRRL 48
|
|
| Tudor_SF |
cd04508 |
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ... |
2227-2279 |
1.19e-04 |
|
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.
Pssm-ID: 410449 [Multi-domain] Cd Length: 47 Bit Score: 41.80 E-value: 1.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2217368908 2227 GTRIAAYWSQQyRCLYPGTVVRGLLDLEddgdlITVEFDDGDTGRIPLSHIRL 2279
Cdd:cd04508 1 GDRVEAKWSDD-GQWYPATVVAVNDDGK-----YTVLFDDGNEEEVSEDDIRP 47
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
251-797 |
3.73e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.40 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 251 QDRGPPRLAERLSPFLAESKTKNAALQPSVLTMCNGGAGDVGLPALVAEAGRGGAKEAARQDEGARLLRRTETLLPGPRP 330
Cdd:COG3321 854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 331 CPSPLPPPPAPPKGPPAPPAATPAGVYTVFREQGREHRVVAPTFVPSVEAFDERPGPIQIASQARDARAREREAGRPGVL 410
Cdd:COG3321 934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 411 QAPPGSPRPLDRPEGLREKNSVIRSLKRPPPADAPTVRATRASPDPRAYVPAKELLKPEADPRPCERAPRGPAGPAAQQA 490
Cdd:COG3321 1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 491 AKLFGLEPGRPPPtgpehkwkpfelgnfAATQMAVLAAQHHHSRAEEEAAVVAASSSKKAYLDPGAVLPRSAATCGRPVA 570
Cdd:COG3321 1094 ALALALAALAAAL---------------LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAA 1158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 571 DMHSAAHGSGEASAMQSLIKYSGSFARDAVAVRPGGCGKKSPFGGLGTMKPEPAPTSAGASRAQARLPHSGGPAAGGGRQ 650
Cdd:COG3321 1159 LAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLAL 1238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 651 LKRDPERPESAKAFGREGSGAQGEAEVRHPPVGIAVAVARQKDSGGSGRLGPGLVDQERSLSLSnVKGHGRADEDCVDDR 730
Cdd:COG3321 1239 AAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALL-AAAAAAAAAAAAAAA 1317
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217368908 731 ARHREERLLGARLDRDQEKLLRESKELADLARLHPTSCAPNGLNPNLMVTGGPALAGSGRWSADPAA 797
Cdd:COG3321 1318 AAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2317-2540 |
3.58e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2317 GGTAGSEEPGAKARGRGRKPSAKAKGDRAATLEEGNPTDEVPSTPLALEPSSTPGSKKSPPEPvdkrakAPKARPAPPQP 2396
Cdd:PRK12323 366 GQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSP------APEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217368908 2397 SPAPPAFTSCPAPEPfaeLPAPATSLAP--APLITMPATRPKPKKARAAEESGAKGPRRPGEEAELLVKLDHEGVTSPKS 2474
Cdd:PRK12323 440 SARGPGGAPAPAPAP---AAAPAAAARPaaAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217368908 2475 KKAKEALLLREDPGAGgwQEPKSLLSLGSYPPAAGSSEPKAPWPKATDGDLAQEPGPGLTFEDSGN 2540
Cdd:PRK12323 517 APAGWVAESIPDPATA--DPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580
|
|
| |
